DCK_BACSU
ID DCK_BACSU Reviewed; 217 AA.
AC P37529;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1994, sequence version 1.
DT 03-AUG-2022, entry version 132.
DE RecName: Full=Deoxyadenosine/deoxycytidine kinase;
DE Short=dAK/dCK;
DE EC=2.7.1.74;
DE EC=2.7.1.76;
GN Name=dck; Synonyms=dak, yaaF; OrderedLocusNames=BSU00140;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=168;
RX PubMed=7584024; DOI=10.1093/dnares/1.1.1;
RA Ogasawara N., Nakai S., Yoshikawa H.;
RT "Systematic sequencing of the 180 kilobase region of the Bacillus subtilis
RT chromosome containing the replication origin.";
RL DNA Res. 1:1-14(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9384377; DOI=10.1038/36786;
RA Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA Yoshikawa H., Danchin A.;
RT "The complete genome sequence of the Gram-positive bacterium Bacillus
RT subtilis.";
RL Nature 390:249-256(1997).
RN [3]
RP FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, SUBSTRATE SPECIFICITY, AND
RP ACTIVITY REGULATION.
RX PubMed=6251049; DOI=10.1016/s0021-9258(19)70633-4;
RA Moellgaard H.;
RT "Deoxyadenosine/deoxycytidine kinase from Bacillus subtilis. Purification,
RT characterization, and physiological function.";
RL J. Biol. Chem. 255:8216-8220(1980).
RN [4]
RP NOMENCLATURE, AND SUBUNIT.
RX PubMed=11078735; DOI=10.1074/jbc.m007918200;
RA Andersen R.B., Neuhard J.;
RT "Deoxynucleoside kinases encoded by the yaaG and yaaF genes of Bacillus
RT subtilis. Substrate specificity and kinetic analysis of deoxyguanosine
RT kinase with UTP as the preferred phosphate donor.";
RL J. Biol. Chem. 276:5518-5524(2001).
CC -!- FUNCTION: Plays an essential role in generating the deoxyribonucleotide
CC precursors dATP AND dCTP for DNA metabolism. The phosphate acceptor
CC specificity is strict toward deoxyadenosine (dAdo) and deoxycytidine
CC (dCyd). The specificity toward the sugar moiety of the nucleoside is
CC less strict. Both 2-deoxyribose, ribose, and arabinose nucleosides are
CC phosphorylated, although the 2-deoxyribonucleosides are preferred. The
CC phosphate donor specificity is dependent on the deoxyribonucleoside
CC substrate, but GTP is efficient with both deoxycytidine and
CC deoxyadenosine. Only nucleoside triphosphates can act as phosphate
CC donors. {ECO:0000269|PubMed:6251049}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2'-deoxyadenosine + ATP = ADP + dAMP + H(+);
CC Xref=Rhea:RHEA:23452, ChEBI:CHEBI:15378, ChEBI:CHEBI:17256,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:58245, ChEBI:CHEBI:456216;
CC EC=2.7.1.76;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2'-deoxycytidine + a ribonucleoside 5'-triphosphate = a
CC ribonucleoside 5'-diphosphate + dCMP + H(+); Xref=Rhea:RHEA:20061,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:15698, ChEBI:CHEBI:57566,
CC ChEBI:CHEBI:57930, ChEBI:CHEBI:61557; EC=2.7.1.74;
CC -!- ACTIVITY REGULATION: Deoxyadenosine inhibits deoxycytidine
CC phosphorylation and deoxycytidine inhibits deoxyadenosine
CC phosphorylation. Deoxyadenosine/deoxycytidine kinase is inhibited by
CC both dATP and dCTP. {ECO:0000269|PubMed:6251049}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=5 uM for deoxyadenosine (with GTP at pH 8.5 and at 37 degrees
CC Celsius) {ECO:0000269|PubMed:6251049};
CC KM=5 uM for deoxycytidine (with GTP at pH 8.5 and at 37 degrees
CC Celsius) {ECO:0000269|PubMed:6251049};
CC KM=65 uM for GTP (with deoxyadenosine or deoxycytidine at pH 7.8 and
CC at 37 degrees Celsius) {ECO:0000269|PubMed:6251049};
CC pH dependence:
CC Optimum pH is around pH 8.6. At pH 8.0-9.6 more than 90% of maximal
CC activity is still observed. {ECO:0000269|PubMed:6251049};
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:11078735}.
CC -!- SIMILARITY: Belongs to the DCK/DGK family. {ECO:0000305}.
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DR EMBL; D26185; BAA05250.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB11790.1; -; Genomic_DNA.
DR PIR; S66044; S66044.
DR RefSeq; NP_387895.1; NC_000964.3.
DR RefSeq; WP_003226792.1; NZ_JNCM01000024.1.
DR AlphaFoldDB; P37529; -.
DR SMR; P37529; -.
DR STRING; 224308.BSU00140; -.
DR PaxDb; P37529; -.
DR PRIDE; P37529; -.
DR EnsemblBacteria; CAB11790; CAB11790; BSU_00140.
DR GeneID; 936793; -.
DR KEGG; bsu:BSU00140; -.
DR PATRIC; fig|224308.179.peg.14; -.
DR eggNOG; COG1428; Bacteria.
DR InParanoid; P37529; -.
DR OMA; EAMVMTP; -.
DR PhylomeDB; P37529; -.
DR BioCyc; BSUB:BSU00140-MON; -.
DR BioCyc; MetaCyc:BSU00140-MON; -.
DR SABIO-RK; P37529; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004136; F:deoxyadenosine kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0004137; F:deoxycytidine kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0019136; F:deoxynucleoside kinase activity; IBA:GO_Central.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd01673; dNK; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR002624; DCK/DGK.
DR InterPro; IPR031314; DNK_dom.
DR InterPro; IPR027417; P-loop_NTPase.
DR Pfam; PF01712; dNK; 1.
DR PIRSF; PIRSF000705; DNK; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Kinase; Nucleotide-binding; Reference proteome; Transferase.
FT CHAIN 1..217
FT /note="Deoxyadenosine/deoxycytidine kinase"
FT /id="PRO_0000049430"
FT ACT_SITE 87
FT /note="Proton acceptor"
FT /evidence="ECO:0000255"
FT BINDING 16..24
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 40
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 52
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 63
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 88
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 93
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 156
FT /ligand="substrate"
FT /evidence="ECO:0000250"
SQ SEQUENCE 217 AA; 25444 MW; B02CDBAA1C518305 CRC64;
MKEHHIPKNS IITVAGTVGV GKSTLTKTLA KRLGFKTSLE EVDHNPYLEK FYHDFERWSF
HLQIYFLAER FKEQKTIFEA GGGFVQDRSI YEDTGIFAKM HADKGTMSKV DYKTYTSLFE
AMVMTPYFPH PDVLIYLEGD LENILNRIEQ RGREMELQTS RSYWEEMHTR YENWISGFNA
CPVLKLRIED YDLLNDENSI ENIVDQIASV IHDNQKK
